| Tag |
Content |
| dbPAF ID |
dbPAF-0000185 |
| Uniprot Accession |
O01583; MRCK_CAEEL;
|
| Genbank Protein ID |
NP_504599.2;
|
| Genbank Nucleotide ID |
NM_072198.5;
|
| Protein Name |
Serine/threonine-protein kinase mrck-1 |
| Protein Synonyms/Alias |
Myotonic dystrophy kinase-related CDC42-binding kinase homolog; |
| Gene Name |
mrck-1 |
| Gene Synonyms/Alias |
K08B12.5; |
| Organism |
Caenorhabditis elegans |
| NCBI Taxa ID |
6239 |
Functional Description
(View all) |
Serine/threonine-protein kinase that may phosphorylate and inactivate the phosphatase mel-11, and thereby contribute to the regulation of myosin II contractility during embryonic elongation (PubMed:19675126). Involved in controlling canal length and Golgi/ER integrity during excretory canal elongation (PubMed:25743393).Functional Description
Serine/threonine-protein kinase that may phosphorylate and inactivate the phosphatase mel-11, and thereby contribute to the regulation of myosin II contractility during embryonic elongation (PubMed:19675126). Involved in controlling canal length and Golgi/ER integrity during excretory canal elongation (PubMed:25743393). |
Phosphorylation Sites
|
dbPAF PTMs: 3 |
Sequence
(Fasta) | MAEPPPDDSA PVRLKTLENI YMDGPSKKPE ALSFETLIDS LICLYDECCN STLRKEKCIA 60
EFVESVKTVI SKAKKLRLSR DDFEVLKVIG KGAFGEVAVV RMRGVGEIYA MKILNKWEMV 120
KRAETACFRE ERDVLVYGDR RWITNLHYAF QDEKNLYFVM DYYIGGDMLT LLSKFVDHIP 180
ESMAKFYIAE MVLAIDSLHR LGYVHRDVKP DNVLLDMQGH IRLADFGSCL RILADGSVAS 240
NVAVGTPDYI SPEILRAMED GRGRYGKECD WWSLGICMYE MLYGTTPFYS ERLVDTYGKI 300
MSHQDMLDFP DDEIDWVVSE EAKDLIRQLI CSSDVRFGRN GLSDFQLHPF FEGIDWNTIR 360
DSNPPYVPEV SSPEDTSNFD VDVCEDDFTP CLQETQPPRV LAAFTGNHLP FVGFSYTHGS 420
LLSDARSLTD EIRAIAQRCQ GDAELMEKSV DGFMVELENE KAELVQKLKE AQTIIAQHVA 480
ENPRSEEDRN YESTIAQLKD EIQILNKRLE DEALAQQQQK PKDEIVAESE KKLKELKERN 540
KQLVMEKSEI QRELDNINDH LDQVLVEKAT VVQQRDDMQA ELADVGDSLL TEKDSVKRLQ 600
DEAEKAKKQV ADFEEKLKEI ETEKIALIKK QEEVTIEARK SVETDDHLSE EVVAAKNTIA 660
SLQATNEERE TEIKKLKQRM DEERASHTAQ SEQEMKQLEA HYERAQKMLQ DNVEQMNVEN 720
RGLRDEIEKL SQQMAALPRG GLNEQQLHEI FNWVSEEKAT REEMENLTRK ITGEVESLKN 780
NSPLTTSNYI QNTPSGWGSR RMNNVARKDG LDLQRQLQAE IDAKLKLKAE LKNSQEQYLT 840
SAARLDDTEK RMASLMREVA MLKQQKNIEN SSDSAFSSTM GRGDLMISMN NDYEMSNSSL 900
MRQEMISRQS TPSYENAILL HDHQVPKRVD DLRYKQKPMK TASGIFSPVS ISAMERGHNF 960
ERMKIKTPTK CGHCTSILIG LDRQGLFCQS CQYACHVSCA ERVSQSCPVP EEERRPLGID 1020
PTRGVGTAYE GLVKTPRAGG VRKGWQTAYV VVCDFKLYLY DCTVDRQNKM QDVKNEIRLV 1080
LDMRDPDFTV CGVSEADVIH AQKGDIPKIF RVTTTQILNS SSEYSSSSKF YTLFMAETEE 1140
EKRKWVVALS ELKTLLRRSK LADRKAFLVK EVFDVTTLPS IRVAQCCAII DRSKIVIGFS 1200
DHGLYCIEIS RQLLIPVGGE KENKQRCVET VEYDEAEQLL MMIVGPAKDR HVRIVPSAAL 1260
DGRDLKWIKV NDTKGCHLLA VGTNNPGGRA GFFAVAFKKS VTIFQIDRSE KRHKKWKDLA 1320
MPGTPQSIAI FNGRLYVGFS HSFRSWSLVG VDSSPVGSGD ASGAVLQHIS LVNMEDTSLQ 1380
FLNQQTSYEA KLIVNVPGSP DEYLLVFNMI GLYVNEMGRR SRLPEVMFPT QAKYFAYHEP 1440
YLCVFSENEV DIFNVTLAEW VQTINLRSAK PLSGDGILST CLCNDSPIFV LLQNVLQDQD 1500
SIEVPVNLAS GSTDGRKVTR RKFTFRTIGK DDRSASERRS HIQISTPSDF MHIVHMGPAP 1560
VMELQQNFID LQSNHSHTSS DKDSLNRSVN ND
1593Fasta Sequence
>O01583|mrck-1|Caenorhabditis elegans
MAEPPPDDSAPVRLKTLENIYMDGPSKKPEALSFETLIDSLICLYDECCNSTLRKEKCIAEFVESVKTVISKAKKLRLSRDDFEVLKVIGKGAFGEVAVVRMRGVGEIYAMKILNKWEMVKRAETACFREERDVLVYGDRRWITNLHYAFQDEKNLYFVMDYYIGGDMLTLLSKFVDHIPESMAKFYIAEMVLAIDSLHRLGYVHRDVKPDNVLLDMQGHIRLADFGSCLRILADGSVASNVAVGTPDYISPEILRAMEDGRGRYGKECDWWSLGICMYEMLYGTTPFYSERLVDTYGKIMSHQDMLDFPDDEIDWVVSEEAKDLIRQLICSSDVRFGRNGLSDFQLHPFFEGIDWNTIRDSNPPYVPEVSSPEDTSNFDVDVCEDDFTPCLQETQPPRVLAAFTGNHLPFVGFSYTHGSLLSDARSLTDEIRAIAQRCQGDAELMEKSVDGFMVELENEKAELVQKLKEAQTIIAQHVAENPRSEEDRNYESTIAQLKDEIQILNKRLEDEALAQQQQKPKDEIVAESEKKLKELKERNKQLVMEKSEIQRELDNINDHLDQVLVEKATVVQQRDDMQAELADVGDSLLTEKDSVKRLQDEAEKAKKQVADFEEKLKEIETEKIALIKKQEEVTIEARKSVETDDHLSEEVVAAKNTIASLQATNEERETEIKKLKQRMDEERASHTAQSEQEMKQLEAHYERAQKMLQDNVEQMNVENRGLRDEIEKLSQQMAALPRGGLNEQQLHEIFNWVSEEKATREEMENLTRKITGEVESLKNNSPLTTSNYIQNTPSGWGSRRMNNVARKDGLDLQRQLQAEIDAKLKLKAELKNSQEQYLTSAARLDDTEKRMASLMREVAMLKQQKNIENSSDSAFSSTMGRGDLMISMNNDYEMSNSSLMRQEMISRQSTPSYENAILLHDHQVPKRVDDLRYKQKPMKTASGIFSPVSISAMERGHNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSCPVPEEERRPLGIDPTRGVGTAYEGLVKTPRAGGVRKGWQTAYVVVCDFKLYLYDCTVDRQNKMQDVKNEIRLVLDMRDPDFTVCGVSEADVIHAQKGDIPKIFRVTTTQILNSSSEYSSSSKFYTLFMAETEEEKRKWVVALSELKTLLRRSKLADRKAFLVKEVFDVTTLPSIRVAQCCAIIDRSKIVIGFSDHGLYCIEISRQLLIPVGGEKENKQRCVETVEYDEAEQLLMMIVGPAKDRHVRIVPSAALDGRDLKWIKVNDTKGCHLLAVGTNNPGGRAGFFAVAFKKSVTIFQIDRSEKRHKKWKDLAMPGTPQSIAIFNGRLYVGFSHSFRSWSLVGVDSSPVGSGDASGAVLQHISLVNMEDTSLQFLNQQTSYEAKLIVNVPGSPDEYLLVFNMIGLYVNEMGRRSRLPEVMFPTQAKYFAYHEPYLCVFSENEVDIFNVTLAEWVQTINLRSAKPLSGDGILSTCLCNDSPIFVLLQNVLQDQDSIEVPVNLASGSTDGRKVTRRKFTFRTIGKDDRSASERRSHIQISTPSDFMHIVHMGPAPVMELQQNFIDLQSNHSHTSSDKDSLNRSVNND
|
| Keyword |
KW-0067--ATP-binding
KW-0175--Coiled coil
KW-0181--Complete proteome
KW-0963--Cytoplasm
KW-0418--Kinase
KW-0460--Magnesium
KW-0479--Metal-binding
KW-0547--Nucleotide-binding
KW-1185--Reference proteome
KW-0723--Serine/threonine-protein kinase
KW-0808--Transferase
KW-0862--Zinc
KW-0863--Zinc-finger
|
| Interpro |
IPR000961--AGC-kinase_C
IPR001180--CNH_dom
IPR000095--CRIB_dom
IPR011009--Kinase-like_dom
IPR002219--PE/DAG-bd
IPR011993--PH/PTB_dom
IPR001849--PH_domain
IPR017892--Pkinase_C
IPR000719--Prot_kinase_dom
IPR017441--Protein_kinase_ATP_BS
IPR002290--Ser/Thr_dual-sp_kinase
IPR008271--Ser/Thr_kinase_AS
|
| PROSITE |
PS51285--AGC_KINASE_CTER
PS50219--CNH
PS50108--CRIB
PS50003--PH_DOMAIN
PS00107--PROTEIN_KINASE_ATP
PS50011--PROTEIN_KINASE_DOM
PS00108--PROTEIN_KINASE_ST
PS00479--ZF_DAG_PE_1
PS50081--ZF_DAG_PE_2
|
| Pfam |
PF00130--C1_1
PF00780--CNH
PF00069--Pkinase
PF00433--Pkinase_C
|
| Gene Ontology |
GO:0005737--C:cytoplasm
GO:0005524--F:ATP binding
GO:0046872--F:metal ion binding
GO:0004674--F:protein serine/threonine kinase activity
GO:0009792--P:embryo development ending in birth or egg hatching
GO:0010172--P:embryonic body morphogenesis
GO:0048598--P:embryonic morphogenesis
GO:0035556--P:intracellular signal transduction
GO:0002119--P:nematode larval development
|
